PDBsum entry 3ask

Ligase/DNA binding protein

PDB id

3ask

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Contents

			Protein chains

					213 a.a.


					154 a.a.

			Ligands

					ALA-ARG-THR-LYS- GLN-THR-ALA-ARG- M3L-SER


					ALA-ARG-THR-LYS- GLN-THR-ALA-ARG- M3L


					M3L

			Metals

					_ZN ×7

			Waters ×4

PDB id:

3ask

Links

Name:

Ligase/DNA binding protein

Title:

Structure of uhrf1 in complex with histone tail

Structure:

E3 ubiquitin-protein ligase uhrf1. Chain: a, b, c, d. Fragment: tandem tudor domain, phd finger (residues 134-366). Engineered: yes. Mutation: yes. Histone h3.3. Chain: p, q, r. Fragment: residues in unp 2-14. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: uhrf1. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606

Resolution:

2.90Å

R-factor:

0.248

R-free:

0.286

Authors:

K.Arita,K.Sugita,M.Unoki,R.Hamamoto,N.Sekiyama,H.Tochio,M.Ariyoshi, M.Shirakawa

Key ref:

K.Arita et al. (2012). Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1. Proc Natl Acad Sci U S A, 109, 12950-12955. PubMed id: 22837395

Date:

16-Dec-10

Release date:

25-Jan-12

PROCHECK

	Headers

	References

Protein chains

Q96T88 (UHRF1_HUMAN) - E3 ubiquitin-protein ligase UHRF1 from Homo sapiens

Seq: Struc:

Seq: Struc:					793 a.a. 213 a.a.*

Protein chains

Q96T88 (UHRF1_HUMAN) - E3 ubiquitin-protein ligase UHRF1 from Homo sapiens

Seq: Struc:

Seq: Struc:					793 a.a. 154 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 2 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

Chains A, B, C, D: E.C.2.3.2.27 - RING-type E3 ubiquitin transferase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N₆- ubiquitinyl-[acceptor protein]-L-lysine

	Proc Natl Acad Sci U S A 109:12950-12955 (2012)
PubMed id: 22837395

Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1.
K.Arita, S.Isogai, T.Oda, M.Unoki, K.Sugita, N.Sekiyama, K.Kuwata, R.Hamamoto, H.Tochio, M.Sato, M.Ariyoshi, M.Shirakawa.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

23211769

C.A.Musselman, M.E.Lalonde, J.Côté, and T.G.Kutateladze (2012).
Perceiving the epigenetic landscape through histone readers.

Nat Struct Mol Biol, 19, 1218-1227.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.